Motion in Endothiapepsin [endopep]

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Classification Known Domain Motion, Shear Mechanism [D-s-2]

Structures
4APE Conformation 1 [ PartsList ]
5ER2 Conformation 2 [ PartsList ]

Description
Small shearing motion at 1 interface between domains (17 degree rotation and 1 Angstrom displacement).

Particular values describing motion
Experimental Methods = x (Traditional x-ray)
Creation Date = 19970822
Modification Date = 19970822

References
A Sali, B Veerapandian, J B Cooper, S I Foundling, D J Hoover and T L Blundell (1989). High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: Analysis of the inhibitor binding and description of the rigid-body shift in the enzyme. EMBO J. 8: 2179-2188. [Medline info for 90005421]
A Sali, B Veerapandian, J B Cooper, D S Moss, T Hofmann and T L Blundell (1992). Domain Flexibility in Aspartic Proteases. Proteins: Struc. Func. Genet. 12: 158-170. [Medline info for 92294166]

GO terms associated with structures
Molecular functionaspartic-type endopeptidase activity, pepsin A activity
Biological processproteolysis and peptidolysis

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Endothiapepsin 4ape [ A ] 5er2 [ E ] 330



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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu